EzCatDB: D00537
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DB codeD00537
RLCP classification1.30.300.2 : Hydrolysis
CATH domainDomain 12.-.-.-
Domain 23.20.20.40 : TIM BarrelCatalytic domain
E.C.3.2.1.91
CSA1qk2

CATH domainRelated DB codes (homologues)
3.20.20.40 : TIM BarrelS00194,D00536

Enzyme Name
UniProtKBKEGG

P07987Q9C1S9
Protein nameExoglucanase 2Exoglucanase-6Acellulose 1,4-beta-cellobiosidase
exo-cellobiohydrolase
beta-1,4-glucan cellobiohydrolase
beta-1,4-glucan cellobiosylhydrolase
1,4-beta-glucan cellobiosidase
exoglucanase
avicelase
CBH 1
C1 cellulase
cellobiohydrolase I
cellobiohydrolase
exo-beta-1,4-glucan cellobiohydrolase
1,4-beta-D-glucan cellobiohydrolase
cellobiosidase
SynonymsEC 3.2.1.91
Exoglucanase II
Exocellobiohydrolase II
CBHII
1,4-beta-cellobiohydrolase
EC 3.2.1.91
Exocellobiohydrolase 6A
1,4-beta-cellobiohydrolase 6A
Beta-glucancellobiohydrolase 6A
Avicelase 2
PfamPF00734 (CBM_1)
PF01341 (Glyco_hydro_6)
[Graphical view]
PF00734 (CBM_1)
PF01341 (Glyco_hydro_6)
[Graphical view]
CAZyGH6 (Glycoside Hydrolase Family)
GH6 (Glycoside Hydrolase Family)

KEGG pathways
MAP codePathways
MAP00500Starch and sucrose metabolism

UniProtKB:Accession NumberP07987Q9C1S9
Entry nameGUX2_TRIREGUX6_HUMIN
ActivityHydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non- reducing ends of the chains.Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non- reducing ends of the chains.
Subunit
Monomer.
Subcellular locationSecreted.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00760C02013C00001C00185C00760
CompoundCelluloseCellotetraoseH2OCellobioseCellulose
TypepolysaccharidepolysaccharideH2Opolysaccharidepolysaccharide
ChEBI
62974
15377
17057

PubChem
439626
962
22247451
439178

             
1cb2AUnboundUnbound UnboundUnbound
1cb2BUnboundUnbound UnboundUnbound
1qjwAUnboundAnalogue:GLC-GLC-SGC-MGL UnboundUnbound
1qjwBUnboundAnalogue:GLC-GLC-SGC-MGL UnboundUnbound
1qk0AUnboundAnalogue:GLC-XYS-IOB UnboundUnbound
1qk0BUnboundAnalogue:GLC-XYS-IOB UnboundUnbound
1qk2AUnboundAnalogue:GLC-GLC-SGC-MGL UnboundUnbound
1qk2BUnboundAnalogue:GLC-GLC-SGC-MGL UnboundUnbound
1bvwAUnboundUnbound UnboundUnbound
2bvwAUnboundUnboundBound:HOH 97Analogue:CTTAnalogue:GLC 602
2bvwBUnboundUnboundBound:HOH 431Analogue:CT3Analogue:GLC 603

Active-site residues
resource
literature [15]
pdbCatalytic residuescomment
          
1cb2AASP 175;ASP 221;ASP 263;ASP 401
mutant Y169F
1cb2BASP 175;ASP 221;ASP 263;ASP 401
mutant Y169F
1qjwAASP 175;ASP 221;ASP 263;ASP 401
mutant Y169F
1qjwBASP 175;ASP 221;ASP 263;ASP 401
mutant Y169F
1qk0AASP 175;ASP 221;ASP 263;ASP 401
 
1qk0BASP 175;ASP 221;ASP 263;ASP 401
 
1qk2AASP 175;ASP 221;ASP 263;ASP 401
 
1qk2BASP 175;ASP 221;ASP 263;ASP 401
 
1bvwAASP 180;ASP 226;ASP 268;ASP 405
 
2bvwAASP 180;ASP 226;ASP 268;ASP 405
 
2bvwBASP 180;ASP 226;ASP 268;ASP 405
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[14]Scheme 11
[15]Fig.6, Fig.7, p.8888-88901

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID90333255
PubMed ID2377893
JournalScience
Year1990
Volume249
Pages380-6
AuthorsRouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA
TitleThree-dimensional structure of cellobiohydrolase II from Trichoderma reesei.
Related UniProtKBP07987
[2]
PubMed ID1761039
JournalEur J Biochem
Year1991
Volume202
Pages367-77
AuthorsGilkes NR, Claeyssens M, Aebersold R, Henrissat B, Meinke A, Morrison HD, Kilburn DG, Warren RA, Miller RC Jr
TitleStructural and functional relationships in two families of beta-1,4-glycanases.
[3]
PubMed ID8399160
JournalBiochemistry
Year1993
Volume32
Pages9906-16
AuthorsSpezio M, Wilson DB, Karplus PA
TitleCrystal structure of the catalytic domain of a thermophilic endocellulase.
[4]
PubMed ID8192865
JournalBiotechnol Appl Biochem
Year1994
Volume19
Pages141-53
AuthorsWoodward J, Brown JP, Evans BR, Affholter KA
TitlePapain digestion of crude Trichoderma reesei cellulase: purification and properties of cellobiohydrolase I and II core proteins.
[5]
PubMed ID7733957
JournalBiochem Biophys Res Commun
Year1995
Volume209
Pages1046-52
AuthorsShultz MD, Lassig JP, Gooch MG, Evans BR, Woodward J
TitlePalladium--a new inhibitor of cellulase activities.
[6]
PubMed ID7857933
JournalBiochemistry
Year1995
Volume34
Pages2220-4
AuthorsDamude HG, Withers SG, Kilburn DG, Miller RC Jr, Warren RA
TitleSite-directed mutation of the putative catalytic residues of endoglucanase CenA from Cellulomonas fimi.
[7]
PubMed ID8615816
JournalBiochem J
Year1996
Volume315
Pages467-72
AuthorsDamude HG, Ferro V, Withers SG, Warren RA
TitleSubstrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6.
[8]
PubMed ID8856058
JournalEur J Biochem
Year1996
Volume240
Pages584-91
AuthorsHarjunpaa V, Teleman A, Koivula A, Ruohonen L, Teeri TT, Teleman O, Drakenberg T
TitleCello-oligosaccharide hydrolysis by cellobiohydrolase II from Trichoderma reesei. Association and rate constants derived from an analysis of progress curves.
[9]
PubMed ID9010760
JournalJ Biochem (Tokyo)
Year1996
Volume120
Pages1123-9
AuthorsAmano Y, Shiroishi M, Nisizawa K, Hoshino E, Kanda T
TitleFine substrate specificities of four exo-type cellulases produced by Aspergillus niger, Trichoderma reesei, and Irpex lacteus on (1-->3), (1-->4)-beta-D-glucans and xyloglucan.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID97029636
PubMed ID8875646
JournalProtein Eng
Year1996
Volume9
Pages691-9
AuthorsKoivula A, Reinikainen T, Ruohonen L, Valkeajarvi A, Claeyssens M, Teleman O, Kleywegt GJ, Szardenings M, Rouvinen J, Jones TA, Teeri TT
TitleThe active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169.
Related PDB1cb2
Related UniProtKBP07987
[11]
PubMed ID8959766
JournalProtein Expr Purif
Year1996
Volume8
Pages399-400
AuthorsKoivula A, Lappalainen A, Virtanen S, Mantyla AL, Suominen P, Teeri TT
TitleImmunoaffinity chromatographic purification of cellobiohydrolase II mutants from recombinant trichoderma reesei strains devoid of major endoglucanase genes.
[12]
PubMed ID9204518
JournalAppl Biochem Biotechnol
Year1997
Volume66
Pages39-56
AuthorsMedve J, Stahlberg J, Tjerneld F
TitleIsotherms for adsorption of cellobiohydrolase I and II from Trichoderma reesei on microcrystalline cellulose.
[13]
CommentsX-ray crystallography
PubMed ID9662445
JournalFEBS Lett
Year1998
Volume429
Pages341-6
AuthorsKoivula A, Kinnari T, Harjunpaa V, Ruohonen L, Teleman A, Drakenberg T, Rouvinen J, Jones TA, Teeri TT
TitleTryptophan 272: an essential determinant of crystalline cellulose degradation by Trichoderma reesei cellobiohydrolase Cel6A.
Related PDB1bvw
[14]
PubMed ID9882628
JournalBiochem J
Year1999
Volume337
Pages297-304
AuthorsVarrot A, Hastrup S, Schulein M, Davies GJ
TitleCrystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution.
[15]
CommentsX-ray crystallography
PubMed ID10413461
JournalBiochemistry
Year1999
Volume38
Pages8884-91
AuthorsVarrot A, Schulein M, Davies GJ
TitleStructural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding.
Related PDB2bvw
[16]
PubMed ID10411622
JournalEur J Biochem
Year1999
Volume262
Pages637-43
AuthorsCarrard G, Linder M
TitleWidely different off rates of two closely related cellulose-binding domains from Trichoderma reesei.
[17]
CommentsX-ray crystallography
PubMed ID10508787
JournalStructure Fold Des
Year1999
Volume7
Pages1035-45
AuthorsZou J, Kleywegt GJ, Stahlberg J, Driguez H, Nerinckx W, Claeyssens M, Koivula A, Teeri TT, Jones TA
TitleCrystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reesei.
Related PDB1qk0,1qk2,1qjw
[18]
PubMed ID10794732
JournalBiochem J
Year2000
Volume348 Pt 1
Pages201-7
AuthorsDavies GJ, Brzozowski AM, Dauter M, Varrot A, Schulein M
TitleStructure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.
[19]
PubMed ID10601873
JournalEur J Biochem
Year2000
Volume267
Pages244-52
AuthorsZhang S, Barr BK, Wilson DB
TitleEffects of noncatalytic residue mutations on substrate specificity and ligand binding of Thermobifida fusca endocellulase cel6A.
[20]
PubMed ID11179652
JournalFEMS Microbiol Lett
Year2001
Volume195
Pages197-204
AuthorsLehtio J, Wernerus H, Samuelson P, Teeri TT, Stahl S
TitleDirected immobilization of recombinant staphylococci on cotton fibers by functional display of a fungal cellulose-binding domain.
[21]
PubMed ID11325554
JournalFEMS Microbiol Lett
Year2001
Volume198
Pages57-63
AuthorsLimon MC, Margolles-Clark E, Benitez T, Penttila M
TitleAddition of substrate-binding domains increases substrate-binding capacity and specific activity of a chitinase from Trichoderma harzianum.
[22]
PubMed ID12007616
JournalBiochim Biophys Acta
Year2002
Volume1596
Pages366-80
AuthorsTuohy MG, Walsh DJ, Murray PG, Claeyssens M, Cuffe MM, Savage AV, Coughlan MP
TitleKinetic parameters and mode of action of the cellobiohydrolases produced by Talaromyces emersonii.
[23]
PubMed ID12188666
JournalJ Am Chem Soc
Year2002
Volume124
Pages10015-24
AuthorsKoivula A, Ruohonen L, Wohlfahrt G, Reinikainen T, Teeri TT, Piens K, Claeyssens M, Weber M, Vasella A, Becker D, Sinnott ML, Zou JY, Kleywegt GJ, Szardenings M, Stahlberg J, Jones TA
TitleThe active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175.
[24]
PubMed ID12565856
JournalBiochem Biophys Res Commun
Year2003
Volume301
Pages280-6
AuthorsMurray PG, Collins CM, Grassick A, Tuohy MG
TitleMolecular cloning, transcriptional, and expression analysis of the first cellulase gene (cbh2), encoding cellobiohydrolase II, from the moderately thermophilic fungus Talaromyces emersonii and structure prediction of the gene product.

comments
This family belongs to Glycosidase family-6, which has an inverting mechanism (equatorial to axial conformation). Furthermore, this enzyme belongs to exoglucanase, which requrires polymer-chain ends for catalytic activity, whilst its family member (EC 3.2.1.4) is endoglucanase.
The literature [7] suggests that endoglucanases from this family-6 may function by different mechanisms from this exoglucanase from the same family.
The literature [15] confirmed that Asp226 (2bvw) atcs as proton donor (acid catalyst) and Asp405 as the catalytic base. In sharp contrast, the literature [6] doubted the role of Asp405, which suggests Asp268 might act as base catalyst. In any case, the identification of catalytic base is difficult for these enzymes.

createdupdated
2002-10-152009-09-29


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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